Aminopeptidases - download pdf or read online

By Allen Taylor Ph.D. (auth.)

ISBN-10: 3662216035

ISBN-13: 9783662216033

ISBN-10: 3662216051

ISBN-13: 9783662216057

This booklet summarizes lately accrued information about the aminopeptidases. Nomenclature, distributions within the plant and animal kingdoms, structural and compositional info, mechanistic reports, homologies, physiological, scientific and business makes use of, and molecular genetics of aminopeptidases are described.

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44 Perturbation of the cobalt spectrum upon binding inhibitors suggests that substrates or inhibitors are within the immediate vicinity of metal ions in Aeromonas AP as well. 33 Bestatin and amastatin are relatively tight-binding inhibitors. , bestatin and amastatin) is a tetrahedral carbon atom positioned between the scissile carbonyl and the carbon which bears the aNH2 group (Fig. 3). This tetrahedral carbon has a hydroxyl which mimics the presumptive tetrahedral transition state which is formed after nucleophilic addition of OH-.

7 44 5. 3 [503] E. 3 640 87 29 17 51 52 86 aminopeptidase P prolidase Continued... 19% with N-terminus of pseudomonas creatinase 53 76 89 p67 and E. 0 (514 residues) 84 50 70 88 Asp, Asp, Glu, His Asp, His Glu Yes Yes 49% identity with arabidopsis AP 5. 5A apart 2 Zn 2+ see biLAP -. I~ I~ [ ~ "0 "'). 3 s· 0 ::> ..... Ill Ill 5· 0:1 0 ::J 0 g. n ::> r:: ::J a.. 4 2 [387, 377 mature] S. Cerevisiae Methionine aminopeptidase 1 Subunit mass (kDa) [#of residues in mature form of protomer] Source Name• #of subunits "'70 "'42 "'34 Total mass (kDa) no metal Co 2• Co 2• Co 2• Metal ion content Cys Cys Residues used to ligand metal ion or active site residues Yes Unique gene?

Thus, there is no significant structural change induced to the enzyme upon binding of LeuP. The same pertains to binding of other inhibitors including bestatin, [(2S,3R)-3-amino2-hydroxy-4-phenylbutanoyl]-L-leucine, and amastatin, [(2S,3R)-3amino-2-hydroxy-5-methylhexanoyl]-L-valyl-L-valyl-aspartic acid, 12 as well (see the next section). The shape of blLAP protomers and their arrangement within the highly homologous porcine kidney (hk 13) LAP hexamer is indistinguishable from that described for the bovine enzyme, although hkLAP crystallized in the space group P2 12 12 1• 14 Unit cell parameters for hkLAP are: a = 186 A, b = 223 A, and c = 80 A.

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Aminopeptidases by Allen Taylor Ph.D. (auth.)


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